Structure of the apo MET receptor kinase in the dually-phosphorylated, activated state. Determined by X-ray diffraction at 1.6 Å resolution. Released 19 Jan 2011.
Explore 3Q6U in 3D Show helices and sheets RCSB PDB PDBe
3Q6U contains 19 α-helices and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1048-1050 | 3 | |
| α-helix | 1055-1057 | 3 | |
| α-helix | 1060-1067 | 8 | |
| β-strand | 1070 | 1 | 1 |
| α-helix | 1073-1075 | 3 | |
| β-strand | 1076-1086 | 11 | 1 |
| β-strand | 1090-1098 | 9 | 1 |
| β-strand | 1104-1112 | 9 | 1 |
| α-helix | 1118-1129 | 12 | |
| β-strand | 1139 | 1 | 2 |
| β-strand | 1144-1146 | 3 | 1 |
| β-strand | 1154-1158 | 5 | 1 |
| β-strand | 1164 | 1 | 2 |
| α-helix | 1165-1170 | 6 | |
| α-helix | 1178-1197 | 20 | |
| α-helix | 1207-1209 | 3 | |
| β-strand | 1210-1212 | 3 | 2 |
| β-strand | 1218-1220 | 3 | 2 |
| α-helix | 1247-1249 | 3 | |
| α-helix | 1252-1257 | 6 | |
| α-helix | 1262-1277 | 16 | |
| α-helix | 1281-1282 | 2 | |
| α-helix | 1289-1291 | 3 | |
| α-helix | 1292-1297 | 6 | |
| α-helix | 1302-1305 | 4 | |
| α-helix | 1310-1319 | 10 | |
| α-helix | 1324-1326 | 3 | |
| α-helix | 1328-1329 | 2 | |
| α-helix | 1330-1343 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hepatocyte growth factor receptor | A | protein | 308 | Homo sapiens | P08581 (AlphaFold model) |
>3Q6U_1 Hepatocyte growth factor receptor (chains A) MQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIH CAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLR NFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLA RDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPD VNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG EHHHHHHH
Structural basis for selective small molecule kinase inhibition of activated c-Met. Rickert, K.W., Patel, S.B., Allison, T.J. et al. J Biol Chem (2011) 286:11218-11225. DOI 10.1074/jbc.M110.204404 · PubMed
Other PDB entries of the same protein (UniProt P08581 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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